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HEADER HYDROLASE 30-SEP-13 4C88
TITLE ESTERASE LPEST1 FROM LACTOBACILLUS PLANTARUM: NATIVE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CARBOXYLESTERASE LPEST1;
COMPND 5 EC: 3.1.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS PLANTARUM;
SOURCE 3 ORGANISM_TAXID: 220668;
SOURCE 4 STRAIN: WCFS1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ALVAREZ,M.ESTEBAN-TORRES,A.CORTES-CABRERA,F.GAGO,I.ACEBRON,
AUTHOR 2 R.BENAVENTE,K.MARDO,B.DE-LAS-RIVAS,R.MUNOZ,J.M.MANCHENO
REVDAT 1 02-APR-14 4C88 0
JRNL AUTH Y.ALVAREZ,M.ESTEBAN-TORRES,A.CORTES-CABRERA,F.GAGO,
JRNL AUTH 2 I.ACEBRON,R.BENAVENTE,K.MARDO,B.DE-LAS-RIVAS,R.MUNOZ,
JRNL AUTH 3 J.M.MANCHENO
JRNL TITL ESTERASE LPEST1 FROM LACTOBACILLUS PLANTARUM: A NOVEL AND
JRNL TITL 2 ATYPICAL MEMBER OF THE ALPHA BETA HYDROLASE SUPERFAMILY OF
JRNL TITL 3 ENZYMES
JRNL REF PLOS ONE V. 9 92257 2014
JRNL REFN ISSN 1932-6203
JRNL PMID 24663330
JRNL DOI 10.1371/JOURNAL.PONE.0092257
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.650
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.678
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.34
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.99
REMARK 3 NUMBER OF REFLECTIONS : 74256
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1384
REMARK 3 R VALUE (WORKING SET) : 0.1371
REMARK 3 FREE R VALUE : 0.1749
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 3737
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 35.9916 - 7.1757 0.95 3590 191 0.1747 0.1720
REMARK 3 2 7.1757 - 5.7029 0.95 3551 190 0.1622 0.1935
REMARK 3 3 5.7029 - 4.9841 0.95 3526 176 0.1307 0.1536
REMARK 3 4 4.9841 - 4.5294 0.95 3544 181 0.1149 0.1391
REMARK 3 5 4.5294 - 4.2053 0.94 3507 207 0.1113 0.1507
REMARK 3 6 4.2053 - 3.9576 0.95 3509 166 0.1104 0.1570
REMARK 3 7 3.9576 - 3.7597 0.95 3519 204 0.1157 0.1585
REMARK 3 8 3.7597 - 3.5962 0.95 3537 188 0.1182 0.1494
REMARK 3 9 3.5962 - 3.4578 0.95 3531 188 0.1251 0.1679
REMARK 3 10 3.4578 - 3.3386 0.95 3516 185 0.1338 0.1485
REMARK 3 11 3.3386 - 3.2343 0.95 3517 179 0.1377 0.1657
REMARK 3 12 3.2343 - 3.1419 0.95 3550 171 0.1335 0.1847
REMARK 3 13 3.1419 - 3.0592 0.95 3476 189 0.1385 0.2003
REMARK 3 14 3.0592 - 2.9846 0.95 3548 190 0.1447 0.1999
REMARK 3 15 2.9846 - 2.9168 0.95 3510 192 0.1513 0.1967
REMARK 3 16 2.9168 - 2.8547 0.94 3481 205 0.1496 0.2017
REMARK 3 17 2.8547 - 2.7977 0.95 3531 176 0.1558 0.2391
REMARK 3 18 2.7977 - 2.7449 0.95 3497 180 0.1559 0.2079
REMARK 3 19 2.7449 - 2.6959 0.95 3560 187 0.1604 0.2406
REMARK 3 20 2.6959 - 2.6502 0.95 3484 192 0.1687 0.2481
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.04
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.9
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.5
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: 0.030
REMARK 3 OPERATOR: -H,K,-L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 10751
REMARK 3 ANGLE : 0.960 14771
REMARK 3 CHIRALITY : 0.068 1713
REMARK 3 PLANARITY : 0.005 1960
REMARK 3 DIHEDRAL : 14.075 3801
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID 0 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.1521 48.8860 -8.8931
REMARK 3 T TENSOR
REMARK 3 T11: 0.2154 T22: 0.2345
REMARK 3 T33: 0.2115 T12: -0.0928
REMARK 3 T13: -0.0679 T23: -0.0321
REMARK 3 L TENSOR
REMARK 3 L11: 3.7720 L22: 1.7912
REMARK 3 L33: 2.7732 L12: -0.1029
REMARK 3 L13: -1.3697 L23: 0.4990
REMARK 3 S TENSOR
REMARK 3 S11: 0.1838 S12: 0.1393 S13: 0.1442
REMARK 3 S21: -0.1374 S22: 0.1211 S23: -0.2104
REMARK 3 S31: -0.4893 S32: 0.2528 S33: -0.2381
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESID 43 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.1622 34.4154 -5.3073
REMARK 3 T TENSOR
REMARK 3 T11: 0.1155 T22: 0.2996
REMARK 3 T33: 0.2846 T12: -0.0363
REMARK 3 T13: 0.0622 T23: -0.0475
REMARK 3 L TENSOR
REMARK 3 L11: 4.3527 L22: 6.3473
REMARK 3 L33: 7.3369 L12: 4.8425
REMARK 3 L13: 5.2951 L23: 5.5480
REMARK 3 S TENSOR
REMARK 3 S11: 0.4135 S12: -0.6210 S13: 0.5332
REMARK 3 S21: 0.5005 S22: -0.4533 S23: 0.0536
REMARK 3 S31: 0.4062 S32: -0.4635 S33: 0.0743
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESID 59 THROUGH 166 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.4376 30.7254 -28.7105
REMARK 3 T TENSOR
REMARK 3 T11: 0.1907 T22: 0.1824
REMARK 3 T33: 0.1106 T12: -0.0256
REMARK 3 T13: -0.0278 T23: -0.0414
REMARK 3 L TENSOR
REMARK 3 L11: 0.7927 L22: 3.1189
REMARK 3 L33: 0.9480 L12: 0.0674
REMARK 3 L13: -0.1514 L23: -0.3347
REMARK 3 S TENSOR
REMARK 3 S11: 0.0273 S12: 0.2146 S13: -0.0333
REMARK 3 S21: -0.4776 S22: 0.0011 S23: -0.0015
REMARK 3 S31: 0.0935 S32: 0.0964 S33: 0.0034
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESID 167 THROUGH 249 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.8331 31.0582 -9.3125
REMARK 3 T TENSOR
REMARK 3 T11: 0.1397 T22: 0.1631
REMARK 3 T33: 0.1413 T12: -0.0268
REMARK 3 T13: -0.0482 T23: -0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 0.1775 L22: 1.6538
REMARK 3 L33: 1.0448 L12: 0.0667
REMARK 3 L13: -0.0075 L23: 1.0559
REMARK 3 S TENSOR
REMARK 3 S11: -0.0214 S12: -0.0760 S13: 0.1029
REMARK 3 S21: 0.1799 S22: 0.0718 S23: -0.1205
REMARK 3 S31: 0.1264 S32: 0.1361 S33: -0.0586
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESID 250 THROUGH 285 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.5041 24.5738 -10.2463
REMARK 3 T TENSOR
REMARK 3 T11: 0.1500 T22: 0.1896
REMARK 3 T33: 0.1316 T12: 0.0435
REMARK 3 T13: -0.0574 T23: -0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 1.7371 L22: 4.5724
REMARK 3 L33: 1.9551 L12: 1.2328
REMARK 3 L13: -0.6300 L23: -0.1252
REMARK 3 S TENSOR
REMARK 3 S11: 0.0633 S12: 0.0502 S13: -0.2727
REMARK 3 S21: 0.3549 S22: -0.0794 S23: -0.3289
REMARK 3 S31: 0.3364 S32: 0.2954 S33: 0.0391
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESID 286 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.1640 39.2360 -14.9782
REMARK 3 T TENSOR
REMARK 3 T11: 0.1079 T22: 0.2144
REMARK 3 T33: 0.1735 T12: -0.0684
REMARK 3 T13: -0.0185 T23: -0.0296
REMARK 3 L TENSOR
REMARK 3 L11: 1.3805 L22: 1.9642
REMARK 3 L33: 2.3425 L12: -0.4101
REMARK 3 L13: 0.3010 L23: 0.1884
REMARK 3 S TENSOR
REMARK 3 S11: 0.0900 S12: -0.0323 S13: 0.0368
REMARK 3 S21: -0.0033 S22: -0.0564 S23: -0.2908
REMARK 3 S31: -0.1069 S32: 0.2949 S33: -0.0314
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND (RESID 1 THROUGH 31 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.4938 35.1152 17.6514
REMARK 3 T TENSOR
REMARK 3 T11: 0.3040 T22: 0.1638
REMARK 3 T33: 0.1250 T12: -0.0657
REMARK 3 T13: -0.0350 T23: -0.1272
REMARK 3 L TENSOR
REMARK 3 L11: 2.2688 L22: 2.9743
REMARK 3 L33: 6.6152 L12: -0.7895
REMARK 3 L13: 1.8271 L23: -3.2004
REMARK 3 S TENSOR
REMARK 3 S11: 0.0971 S12: 0.2067 S13: -0.2384
REMARK 3 S21: -0.2210 S22: -0.3496 S23: -0.0662
REMARK 3 S31: 0.5513 S32: 0.6175 S33: -0.1221
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND (RESID 32 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.4369 43.5159 42.3381
REMARK 3 T TENSOR
REMARK 3 T11: 0.2379 T22: 0.2445
REMARK 3 T33: 0.1539 T12: 0.0104
REMARK 3 T13: -0.0643 T23: 0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 1.0750 L22: 5.0576
REMARK 3 L33: 2.1086 L12: 0.6587
REMARK 3 L13: 0.3640 L23: 1.6335
REMARK 3 S TENSOR
REMARK 3 S11: 0.1290 S12: -0.2367 S13: -0.1035
REMARK 3 S21: 0.5674 S22: -0.0441 S23: -0.1172
REMARK 3 S31: 0.0131 S32: -0.1483 S33: -0.1108
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN B AND (RESID 59 THROUGH 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): 59.9930 58.7480 24.5626
REMARK 3 T TENSOR
REMARK 3 T11: 0.2092 T22: 0.1762
REMARK 3 T33: 0.1987 T12: -0.0802
REMARK 3 T13: -0.0840 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 1.5509 L22: 2.7907
REMARK 3 L33: 0.9650 L12: -1.0000
REMARK 3 L13: -0.5350 L23: 1.0224
REMARK 3 S TENSOR
REMARK 3 S11: -0.0710 S12: 0.0027 S13: 0.2689
REMARK 3 S21: -0.0117 S22: -0.0223 S23: -0.3103
REMARK 3 S31: -0.2897 S32: 0.3308 S33: -0.0441
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN B AND (RESID 129 THROUGH 249 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.6068 56.9054 27.1130
REMARK 3 T TENSOR
REMARK 3 T11: 0.1508 T22: 0.1223
REMARK 3 T33: 0.1089 T12: -0.0458
REMARK 3 T13: -0.0346 T23: -0.0193
REMARK 3 L TENSOR
REMARK 3 L11: 0.6469 L22: 1.5071
REMARK 3 L33: 0.8842 L12: -0.4689
REMARK 3 L13: 0.3616 L23: 0.3555
REMARK 3 S TENSOR
REMARK 3 S11: 0.0022 S12: -0.0539 S13: 0.0746
REMARK 3 S21: 0.1071 S22: -0.0284 S23: -0.0394
REMARK 3 S31: -0.1179 S32: -0.0316 S33: 0.0253
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND (RESID 250 THROUGH 285 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.8877 57.6142 25.6410
REMARK 3 T TENSOR
REMARK 3 T11: 0.1131 T22: 0.1659
REMARK 3 T33: 0.1282 T12: -0.0358
REMARK 3 T13: -0.0687 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 0.8603 L22: 4.2775
REMARK 3 L33: 1.6166 L12: -0.3562
REMARK 3 L13: -1.0333 L23: 1.4404
REMARK 3 S TENSOR
REMARK 3 S11: 0.1171 S12: 0.1692 S13: 0.1138
REMARK 3 S21: 0.0549 S22: 0.0018 S23: 0.2062
REMARK 3 S31: -0.0628 S32: -0.2719 S33: -0.0184
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN B AND (RESID 286 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.2184 46.2980 20.6106
REMARK 3 T TENSOR
REMARK 3 T11: 0.1526 T22: 0.1171
REMARK 3 T33: 0.1210 T12: -0.0588
REMARK 3 T13: -0.0267 T23: -0.0484
REMARK 3 L TENSOR
REMARK 3 L11: 1.5162 L22: 1.9785
REMARK 3 L33: 1.3582 L12: -0.2475
REMARK 3 L13: 0.1241 L23: -0.6490
REMARK 3 S TENSOR
REMARK 3 S11: 0.0517 S12: -0.0362 S13: -0.0607
REMARK 3 S21: -0.1040 S22: -0.0649 S23: 0.0135
REMARK 3 S31: 0.0240 S32: -0.0371 S33: 0.0053
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN C AND (RESID 1 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.9835 55.9862 -23.6503
REMARK 3 T TENSOR
REMARK 3 T11: 0.1694 T22: 0.1324
REMARK 3 T33: 0.1969 T12: 0.0079
REMARK 3 T13: -0.0453 T23: -0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 2.1491 L22: 1.8345
REMARK 3 L33: 3.1173 L12: 0.5495
REMARK 3 L13: -0.6172 L23: 0.8933
REMARK 3 S TENSOR
REMARK 3 S11: 0.0015 S12: -0.1252 S13: 0.1815
REMARK 3 S21: 0.0355 S22: 0.0333 S23: -0.2041
REMARK 3 S31: -0.2341 S32: 0.3958 S33: -0.0839
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN C AND (RESID 59 THROUGH 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1402 33.9549 -19.1653
REMARK 3 T TENSOR
REMARK 3 T11: 0.1415 T22: 0.1337
REMARK 3 T33: 0.2345 T12: -0.0379
REMARK 3 T13: 0.0293 T23: -0.0594
REMARK 3 L TENSOR
REMARK 3 L11: 3.9412 L22: 0.7499
REMARK 3 L33: 1.2968 L12: -0.5669
REMARK 3 L13: 1.5821 L23: 0.2820
REMARK 3 S TENSOR
REMARK 3 S11: 0.0032 S12: -0.0276 S13: -0.4628
REMARK 3 S21: 0.0954 S22: -0.0118 S23: 0.1434
REMARK 3 S31: 0.1743 S32: 0.0274 S33: -0.0279
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN C AND (RESID 129 THROUGH 249 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7074 47.9380 -21.4307
REMARK 3 T TENSOR
REMARK 3 T11: 0.1261 T22: 0.1088
REMARK 3 T33: 0.1198 T12: 0.0103
REMARK 3 T13: -0.0016 T23: -0.0643
REMARK 3 L TENSOR
REMARK 3 L11: 2.0990 L22: 1.0137
REMARK 3 L33: 1.3241 L12: 0.5185
REMARK 3 L13: -0.3501 L23: -0.1843
REMARK 3 S TENSOR
REMARK 3 S11: -0.0148 S12: -0.0238 S13: 0.0200
REMARK 3 S21: 0.0159 S22: 0.0271 S23: -0.0122
REMARK 3 S31: -0.0920 S32: -0.1159 S33: -0.0105
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN C AND (RESID 250 THROUGH 285 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.8175 54.3538 -20.1510
REMARK 3 T TENSOR
REMARK 3 T11: 0.1939 T22: 0.1241
REMARK 3 T33: 0.2091 T12: 0.0466
REMARK 3 T13: 0.0294 T23: -0.0740
REMARK 3 L TENSOR
REMARK 3 L11: 2.4734 L22: 1.3423
REMARK 3 L33: 2.4376 L12: 1.3179
REMARK 3 L13: 0.8336 L23: -0.3294
REMARK 3 S TENSOR
REMARK 3 S11: -0.0038 S12: -0.0837 S13: 0.3481
REMARK 3 S21: 0.1494 S22: 0.0116 S23: 0.0997
REMARK 3 S31: -0.3176 S32: -0.3319 S33: -0.0423
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN C AND (RESID 286 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7388 52.1551 -15.1017
REMARK 3 T TENSOR
REMARK 3 T11: 0.1911 T22: 0.1325
REMARK 3 T33: 0.1564 T12: -0.0356
REMARK 3 T13: -0.0305 T23: -0.0716
REMARK 3 L TENSOR
REMARK 3 L11: 1.6450 L22: 1.4406
REMARK 3 L33: 1.6818 L12: 0.3942
REMARK 3 L13: -0.3307 L23: -0.2539
REMARK 3 S TENSOR
REMARK 3 S11: 0.1236 S12: -0.2486 S13: 0.0977
REMARK 3 S21: 0.0368 S22: -0.1277 S23: 0.0004
REMARK 3 S31: -0.1879 S32: 0.0038 S33: 0.0175
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN D AND (RESID 0 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.1435 99.8133 13.1366
REMARK 3 T TENSOR
REMARK 3 T11: 0.4022 T22: 0.3138
REMARK 3 T33: 0.3495 T12: 0.0546
REMARK 3 T13: -0.1309 T23: 0.0521
REMARK 3 L TENSOR
REMARK 3 L11: 2.3716 L22: 1.5398
REMARK 3 L33: 1.2931 L12: -0.2087
REMARK 3 L13: 0.9414 L23: 0.0699
REMARK 3 S TENSOR
REMARK 3 S11: -0.0885 S12: 0.0816 S13: 0.3630
REMARK 3 S21: -0.5095 S22: 0.0337 S23: 0.5062
REMARK 3 S31: -0.2594 S32: -0.2970 S33: 0.0542
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN D AND (RESID 59 THROUGH 166 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.4721 90.0712 34.1403
REMARK 3 T TENSOR
REMARK 3 T11: 0.1435 T22: 0.1538
REMARK 3 T33: 0.1086 T12: -0.0261
REMARK 3 T13: -0.0203 T23: 0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 1.7946 L22: 3.2252
REMARK 3 L33: 1.3003 L12: -1.0318
REMARK 3 L13: -0.5082 L23: 0.7108
REMARK 3 S TENSOR
REMARK 3 S11: -0.0435 S12: -0.1262 S13: -0.1321
REMARK 3 S21: 0.3140 S22: 0.0321 S23: 0.1679
REMARK 3 S31: 0.0685 S32: -0.0519 S33: 0.0076
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN D AND (RESID 167 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.6261 87.2457 16.7452
REMARK 3 T TENSOR
REMARK 3 T11: 0.2829 T22: 0.2279
REMARK 3 T33: 0.2499 T12: -0.0265
REMARK 3 T13: -0.1258 T23: -0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 1.0001 L22: 1.7616
REMARK 3 L33: 1.4235 L12: -0.2374
REMARK 3 L13: -0.0708 L23: -0.0142
REMARK 3 S TENSOR
REMARK 3 S11: -0.0079 S12: 0.2044 S13: -0.0222
REMARK 3 S21: -0.5638 S22: 0.0217 S23: 0.4218
REMARK 3 S31: 0.0051 S32: -0.2200 S33: -0.0331
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4C88 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-SEP-13.
REMARK 100 THE PDBE ID CODE IS EBI-58530.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.94000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74256
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.65
REMARK 200 RESOLUTION RANGE LOW (A) : 53.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.3
REMARK 200 R MERGE (I) : 0.16
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.3
REMARK 200 R MERGE FOR SHELL (I) : 0.51
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.8 M SODIUM ACETATE TRIHYDRATE
REMARK 280 PH 7.0 AND 35%(V/V) TACSIMATE PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 8555 Y+1/2,-X+1/2,Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 84.17000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 84.17000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 92.10000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 84.17000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 84.17000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 92.10000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 84.17000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 84.17000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 92.10000
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 84.17000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 84.17000
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 92.10000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -16
REMARK 465 GLY A -15
REMARK 465 SER A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 GLY A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 GLY B -16
REMARK 465 GLY B -15
REMARK 465 SER B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 GLY B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
REMARK 465 GLY B 0
REMARK 465 GLY C -16
REMARK 465 GLY C -15
REMARK 465 SER C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 GLY C -7
REMARK 465 GLU C -6
REMARK 465 ASN C -5
REMARK 465 LEU C -4
REMARK 465 TYR C -3
REMARK 465 PHE C -2
REMARK 465 GLY D -16
REMARK 465 GLY D -15
REMARK 465 SER D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 HIS D -9
REMARK 465 HIS D -8
REMARK 465 GLY D -7
REMARK 465 GLU D -6
REMARK 465 ASN D -5
REMARK 465 LEU D -4
REMARK 465 TYR D -3
REMARK 465 PHE D -2
REMARK 465 GLN D -1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OH TYR A 234 O HOH A 2392 2.11
REMARK 500 O GLN B 93 O HOH B 2243 2.16
REMARK 500 OE1 GLU B 160 O HOH B 2313 2.19
REMARK 500 OG1 THR B 301 O HOH B 2412 2.17
REMARK 500 O ASP C 163 NH2B ARG C 194 2.09
REMARK 500 O THR C 166 NH1B ARG C 194 2.05
REMARK 500 OG1 THR C 301 O HOH C 2402 2.12
REMARK 500 OG1 THR D 166 O HOH D 2166 2.14
REMARK 500 O HOH A 2065 O HOH A 2401 2.18
REMARK 500 O HOH A 2074 O HOH A 2121 2.12
REMARK 500 O HOH A 2142 O HOH A 2294 2.16
REMARK 500 O HOH A 2184 O HOH A 2185 2.05
REMARK 500 O HOH A 2195 O HOH A 2293 2.16
REMARK 500 O HOH A 2238 O HOH A 2240 2.18
REMARK 500 O HOH A 2262 O HOH A 2440 2.03
REMARK 500 O HOH A 2270 O HOH A 2323 2.16
REMARK 500 O HOH B 2021 O HOH A 2366 2.16
REMARK 500 O HOH B 2026 O HOH B 2028 2.10
REMARK 500 O HOH B 2066 O HOH B 2235 2.19
REMARK 500 O HOH B 2067 O HOH B 2154 2.20
REMARK 500 O HOH B 2140 O HOH B 2141 2.15
REMARK 500 O HOH B 2196 O HOH B 2200 2.17
REMARK 500 O HOH B 2199 O HOH B 2200 2.20
REMARK 500 O HOH B 2265 O HOH B 2428 2.17
REMARK 500 O HOH B 2396 O HOH B 2398 2.17
REMARK 500 O HOH C 2004 O HOH A 2071 2.19
REMARK 500 O HOH C 2069 O HOH C 2119 2.06
REMARK 500 O HOH C 2177 O HOH C 2178 2.12
REMARK 500 O HOH C 2178 O HOH C 2325 2.17
REMARK 500 O HOH C 2180 O HOH C 2275 2.16
REMARK 500 O HOH C 2404 O HOH C 2407 2.19
REMARK 500 O HOH D 2001 O HOH D 2002 2.11
REMARK 500 O HOH D 2118 O HOH D 2119 2.15
REMARK 500 O HOH D 2119 O HOH D 2314 2.11
REMARK 500 O HOH D 2148 O HOH D 2282 2.13
REMARK 500 O HOH D 2232 O HOH D 2296 2.16
REMARK 500 O HOH D 2308 O HOH D 2309 2.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 N MET B 1 O HOH D 2320 3655 2.15
REMARK 500 O GLN B 93 O HOH D 2092 3655 2.18
REMARK 500 OD2 ASP D 50 O HOH B 2289 4565 2.19
REMARK 500 O HOH B 2008 O HOH D 2099 3655 2.19
REMARK 500 O HOH B 2083 O HOH D 2147 3655 2.16
REMARK 500 O HOH D 2113 O HOH C 2126 7555 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 HIS A 98 -56.10 73.80
REMARK 500 PHE A 109 -27.70 74.28
REMARK 500 SER A 174 -122.23 56.25
REMARK 500 TYR A 202 62.04 35.24
REMARK 500 ALA A 206 73.58 -152.85
REMARK 500 ASN A 312 -148.56 -111.91
REMARK 500 ASN B 94 81.46 55.73
REMARK 500 HIS B 98 -39.91 75.62
REMARK 500 PHE B 109 -28.09 71.45
REMARK 500 SER B 174 -124.65 54.67
REMARK 500 TYR B 202 62.85 34.88
REMARK 500 ALA B 206 78.28 -158.45
REMARK 500 ASN B 312 -150.09 -110.25
REMARK 500 ASN C 94 85.19 54.29
REMARK 500 HIS C 98 -17.49 71.40
REMARK 500 PHE C 109 -33.41 72.95
REMARK 500 SER C 174 -126.13 60.60
REMARK 500 TYR C 202 64.96 36.87
REMARK 500 ALA C 206 75.56 -151.59
REMARK 500 ASN C 312 -153.15 -106.23
REMARK 500 HIS D 98 -57.55 77.76
REMARK 500 PHE D 109 -28.75 73.04
REMARK 500 ASN D 117 24.51 -143.92
REMARK 500 SER D 174 -130.20 58.91
REMARK 500 TYR D 202 67.64 31.88
REMARK 500 ALA D 206 75.79 -151.40
REMARK 500 ASN D 312 -154.67 -108.36
REMARK 500 ALA D 314 31.97 70.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4C87 RELATED DB: PDB
REMARK 900 ESTERASE LPEST1 FROM LACTOBACILLUS PLANTARUM WCFS1
REMARK 900 RELATED ID: 4C89 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CARBOXYLESTERASE LPEST1 FROM
REMARK 900 LACTOBACILLUS PLANTARUM: HIGH RESOLUTION MODEL
DBREF 4C88 A 1 337 UNP Q88Y25 Q88Y25_LACPN 1 337
DBREF 4C88 B 1 337 UNP Q88Y25 Q88Y25_LACPN 1 337
DBREF 4C88 C 1 337 UNP Q88Y25 Q88Y25_LACPN 1 337
DBREF 4C88 D 1 337 UNP Q88Y25 Q88Y25_LACPN 1 337
SEQADV 4C88 GLY A -16 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLY A -15 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 SER A -14 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS A -13 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS A -12 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS A -11 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS A -10 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS A -9 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS A -8 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLY A -7 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLU A -6 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 ASN A -5 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 LEU A -4 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 TYR A -3 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 PHE A -2 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLN A -1 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLY A 0 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLY B -16 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLY B -15 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 SER B -14 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS B -13 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS B -12 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS B -11 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS B -10 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS B -9 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS B -8 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLY B -7 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLU B -6 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 ASN B -5 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 LEU B -4 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 TYR B -3 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 PHE B -2 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLN B -1 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLY B 0 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLY C -16 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLY C -15 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 SER C -14 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS C -13 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS C -12 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS C -11 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS C -10 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS C -9 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS C -8 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLY C -7 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLU C -6 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 ASN C -5 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 LEU C -4 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 TYR C -3 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 PHE C -2 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLN C -1 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLY C 0 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLY D -16 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLY D -15 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 SER D -14 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS D -13 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS D -12 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS D -11 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS D -10 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS D -9 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 HIS D -8 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLY D -7 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLU D -6 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 ASN D -5 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 LEU D -4 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 TYR D -3 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 PHE D -2 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLN D -1 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C88 GLY D 0 UNP Q88Y25 EXPRESSION TAG
SEQRES 1 A 354 GLY GLY SER HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU
SEQRES 2 A 354 TYR PHE GLN GLY MET PRO THR ILE ASN SER ILE GLN THR
SEQRES 3 A 354 THR VAL ASN GLY VAL VAL LYS ILE VAL LYS PRO PHE ASN
SEQRES 4 A 354 ASN ASP ILE ALA GLY GLU GLN PHE ASP PRO HIS VAL LEU
SEQRES 5 A 354 GLN THR LEU THR ALA PHE LYS GLN PRO ALA ILE LEU GLU
SEQRES 6 A 354 ASN ASP LEU ALA ALA LEU ARG SER GLY SER LEU THR PRO
SEQRES 7 A 354 ALA ILE ALA ASP PRO VAL GLY ASP ALA VAL THR VAL GLN
SEQRES 8 A 354 SER ARG ASN ILE THR ALA LEU ASN ARG THR VAL SER VAL
SEQRES 9 A 354 GLU TRP LEU THR PRO GLN ASN VAL ILE ASN HIS THR VAL
SEQRES 10 A 354 LEU VAL TYR PHE HIS GLY GLY ALA PHE TYR GLY GLY VAL
SEQRES 11 A 354 PRO GLY ASN ASN THR VAL LEU LEU LYS LEU VAL ALA ALA
SEQRES 12 A 354 LYS SER HIS CYS GLU ILE LEU ASN VAL ASP TYR SER LEU
SEQRES 13 A 354 ALA PRO GLU ALA PRO ALA PRO ALA GLY ILE LEU ASP GLY
SEQRES 14 A 354 LEU ALA ILE PHE GLN TYR LEU GLU GLN ARG ASP ALA GLU
SEQRES 15 A 354 THR MET ILE THR VAL ALA GLY ASP SER ALA GLY ALA ASN
SEQRES 16 A 354 VAL ILE MET ALA ALA THR ASN LEU ASN GLN GLN LEU GLY
SEQRES 17 A 354 SER ASN ARG ILE ASN GLN GLN LEU LEU LEU TYR PRO VAL
SEQRES 18 A 354 THR ALA PRO ASN ALA ASP HIS ALA GLY PRO LEU TRP ASP
SEQRES 19 A 354 LEU ALA ALA PHE PRO ILE ILE ASP SER GLN ARG ALA ILE
SEQRES 20 A 354 LEU THR ASN TYR HIS ASP LEU PHE ARG GLN LEU ASP SER
SEQRES 21 A 354 ILE MET THR ASP TYR TYR VAL PRO GLU ASN PHE ASP SER
SEQRES 22 A 354 HIS SER PRO LEU ILE SER PRO LEU HIS GLN GLU ASN PHE
SEQRES 23 A 354 THR MET THR PRO PRO THR THR ILE MET VAL GLY GLU PHE
SEQRES 24 A 354 ASP PRO PHE ARG PRO GLN ALA TRP ALA TYR ALA GLN ARG
SEQRES 25 A 354 LEU ALA ALA ALA ASP THR ALA THR THR PHE ILE GLN TYR
SEQRES 26 A 354 GLN GLY LEU ASN HIS ALA PHE ALA PRO LEU VAL ASP GLN
SEQRES 27 A 354 TYR TRP GLN SER GLN ASP VAL ALA GLN VAL MET ALA ALA
SEQRES 28 A 354 ALA LEU ILE
SEQRES 1 B 354 GLY GLY SER HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU
SEQRES 2 B 354 TYR PHE GLN GLY MET PRO THR ILE ASN SER ILE GLN THR
SEQRES 3 B 354 THR VAL ASN GLY VAL VAL LYS ILE VAL LYS PRO PHE ASN
SEQRES 4 B 354 ASN ASP ILE ALA GLY GLU GLN PHE ASP PRO HIS VAL LEU
SEQRES 5 B 354 GLN THR LEU THR ALA PHE LYS GLN PRO ALA ILE LEU GLU
SEQRES 6 B 354 ASN ASP LEU ALA ALA LEU ARG SER GLY SER LEU THR PRO
SEQRES 7 B 354 ALA ILE ALA ASP PRO VAL GLY ASP ALA VAL THR VAL GLN
SEQRES 8 B 354 SER ARG ASN ILE THR ALA LEU ASN ARG THR VAL SER VAL
SEQRES 9 B 354 GLU TRP LEU THR PRO GLN ASN VAL ILE ASN HIS THR VAL
SEQRES 10 B 354 LEU VAL TYR PHE HIS GLY GLY ALA PHE TYR GLY GLY VAL
SEQRES 11 B 354 PRO GLY ASN ASN THR VAL LEU LEU LYS LEU VAL ALA ALA
SEQRES 12 B 354 LYS SER HIS CYS GLU ILE LEU ASN VAL ASP TYR SER LEU
SEQRES 13 B 354 ALA PRO GLU ALA PRO ALA PRO ALA GLY ILE LEU ASP GLY
SEQRES 14 B 354 LEU ALA ILE PHE GLN TYR LEU GLU GLN ARG ASP ALA GLU
SEQRES 15 B 354 THR MET ILE THR VAL ALA GLY ASP SER ALA GLY ALA ASN
SEQRES 16 B 354 VAL ILE MET ALA ALA THR ASN LEU ASN GLN GLN LEU GLY
SEQRES 17 B 354 SER ASN ARG ILE ASN GLN GLN LEU LEU LEU TYR PRO VAL
SEQRES 18 B 354 THR ALA PRO ASN ALA ASP HIS ALA GLY PRO LEU TRP ASP
SEQRES 19 B 354 LEU ALA ALA PHE PRO ILE ILE ASP SER GLN ARG ALA ILE
SEQRES 20 B 354 LEU THR ASN TYR HIS ASP LEU PHE ARG GLN LEU ASP SER
SEQRES 21 B 354 ILE MET THR ASP TYR TYR VAL PRO GLU ASN PHE ASP SER
SEQRES 22 B 354 HIS SER PRO LEU ILE SER PRO LEU HIS GLN GLU ASN PHE
SEQRES 23 B 354 THR MET THR PRO PRO THR THR ILE MET VAL GLY GLU PHE
SEQRES 24 B 354 ASP PRO PHE ARG PRO GLN ALA TRP ALA TYR ALA GLN ARG
SEQRES 25 B 354 LEU ALA ALA ALA ASP THR ALA THR THR PHE ILE GLN TYR
SEQRES 26 B 354 GLN GLY LEU ASN HIS ALA PHE ALA PRO LEU VAL ASP GLN
SEQRES 27 B 354 TYR TRP GLN SER GLN ASP VAL ALA GLN VAL MET ALA ALA
SEQRES 28 B 354 ALA LEU ILE
SEQRES 1 C 354 GLY GLY SER HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU
SEQRES 2 C 354 TYR PHE GLN GLY MET PRO THR ILE ASN SER ILE GLN THR
SEQRES 3 C 354 THR VAL ASN GLY VAL VAL LYS ILE VAL LYS PRO PHE ASN
SEQRES 4 C 354 ASN ASP ILE ALA GLY GLU GLN PHE ASP PRO HIS VAL LEU
SEQRES 5 C 354 GLN THR LEU THR ALA PHE LYS GLN PRO ALA ILE LEU GLU
SEQRES 6 C 354 ASN ASP LEU ALA ALA LEU ARG SER GLY SER LEU THR PRO
SEQRES 7 C 354 ALA ILE ALA ASP PRO VAL GLY ASP ALA VAL THR VAL GLN
SEQRES 8 C 354 SER ARG ASN ILE THR ALA LEU ASN ARG THR VAL SER VAL
SEQRES 9 C 354 GLU TRP LEU THR PRO GLN ASN VAL ILE ASN HIS THR VAL
SEQRES 10 C 354 LEU VAL TYR PHE HIS GLY GLY ALA PHE TYR GLY GLY VAL
SEQRES 11 C 354 PRO GLY ASN ASN THR VAL LEU LEU LYS LEU VAL ALA ALA
SEQRES 12 C 354 LYS SER HIS CYS GLU ILE LEU ASN VAL ASP TYR SER LEU
SEQRES 13 C 354 ALA PRO GLU ALA PRO ALA PRO ALA GLY ILE LEU ASP GLY
SEQRES 14 C 354 LEU ALA ILE PHE GLN TYR LEU GLU GLN ARG ASP ALA GLU
SEQRES 15 C 354 THR MET ILE THR VAL ALA GLY ASP SER ALA GLY ALA ASN
SEQRES 16 C 354 VAL ILE MET ALA ALA THR ASN LEU ASN GLN GLN LEU GLY
SEQRES 17 C 354 SER ASN ARG ILE ASN GLN GLN LEU LEU LEU TYR PRO VAL
SEQRES 18 C 354 THR ALA PRO ASN ALA ASP HIS ALA GLY PRO LEU TRP ASP
SEQRES 19 C 354 LEU ALA ALA PHE PRO ILE ILE ASP SER GLN ARG ALA ILE
SEQRES 20 C 354 LEU THR ASN TYR HIS ASP LEU PHE ARG GLN LEU ASP SER
SEQRES 21 C 354 ILE MET THR ASP TYR TYR VAL PRO GLU ASN PHE ASP SER
SEQRES 22 C 354 HIS SER PRO LEU ILE SER PRO LEU HIS GLN GLU ASN PHE
SEQRES 23 C 354 THR MET THR PRO PRO THR THR ILE MET VAL GLY GLU PHE
SEQRES 24 C 354 ASP PRO PHE ARG PRO GLN ALA TRP ALA TYR ALA GLN ARG
SEQRES 25 C 354 LEU ALA ALA ALA ASP THR ALA THR THR PHE ILE GLN TYR
SEQRES 26 C 354 GLN GLY LEU ASN HIS ALA PHE ALA PRO LEU VAL ASP GLN
SEQRES 27 C 354 TYR TRP GLN SER GLN ASP VAL ALA GLN VAL MET ALA ALA
SEQRES 28 C 354 ALA LEU ILE
SEQRES 1 D 354 GLY GLY SER HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU
SEQRES 2 D 354 TYR PHE GLN GLY MET PRO THR ILE ASN SER ILE GLN THR
SEQRES 3 D 354 THR VAL ASN GLY VAL VAL LYS ILE VAL LYS PRO PHE ASN
SEQRES 4 D 354 ASN ASP ILE ALA GLY GLU GLN PHE ASP PRO HIS VAL LEU
SEQRES 5 D 354 GLN THR LEU THR ALA PHE LYS GLN PRO ALA ILE LEU GLU
SEQRES 6 D 354 ASN ASP LEU ALA ALA LEU ARG SER GLY SER LEU THR PRO
SEQRES 7 D 354 ALA ILE ALA ASP PRO VAL GLY ASP ALA VAL THR VAL GLN
SEQRES 8 D 354 SER ARG ASN ILE THR ALA LEU ASN ARG THR VAL SER VAL
SEQRES 9 D 354 GLU TRP LEU THR PRO GLN ASN VAL ILE ASN HIS THR VAL
SEQRES 10 D 354 LEU VAL TYR PHE HIS GLY GLY ALA PHE TYR GLY GLY VAL
SEQRES 11 D 354 PRO GLY ASN ASN THR VAL LEU LEU LYS LEU VAL ALA ALA
SEQRES 12 D 354 LYS SER HIS CYS GLU ILE LEU ASN VAL ASP TYR SER LEU
SEQRES 13 D 354 ALA PRO GLU ALA PRO ALA PRO ALA GLY ILE LEU ASP GLY
SEQRES 14 D 354 LEU ALA ILE PHE GLN TYR LEU GLU GLN ARG ASP ALA GLU
SEQRES 15 D 354 THR MET ILE THR VAL ALA GLY ASP SER ALA GLY ALA ASN
SEQRES 16 D 354 VAL ILE MET ALA ALA THR ASN LEU ASN GLN GLN LEU GLY
SEQRES 17 D 354 SER ASN ARG ILE ASN GLN GLN LEU LEU LEU TYR PRO VAL
SEQRES 18 D 354 THR ALA PRO ASN ALA ASP HIS ALA GLY PRO LEU TRP ASP
SEQRES 19 D 354 LEU ALA ALA PHE PRO ILE ILE ASP SER GLN ARG ALA ILE
SEQRES 20 D 354 LEU THR ASN TYR HIS ASP LEU PHE ARG GLN LEU ASP SER
SEQRES 21 D 354 ILE MET THR ASP TYR TYR VAL PRO GLU ASN PHE ASP SER
SEQRES 22 D 354 HIS SER PRO LEU ILE SER PRO LEU HIS GLN GLU ASN PHE
SEQRES 23 D 354 THR MET THR PRO PRO THR THR ILE MET VAL GLY GLU PHE
SEQRES 24 D 354 ASP PRO PHE ARG PRO GLN ALA TRP ALA TYR ALA GLN ARG
SEQRES 25 D 354 LEU ALA ALA ALA ASP THR ALA THR THR PHE ILE GLN TYR
SEQRES 26 D 354 GLN GLY LEU ASN HIS ALA PHE ALA PRO LEU VAL ASP GLN
SEQRES 27 D 354 TYR TRP GLN SER GLN ASP VAL ALA GLN VAL MET ALA ALA
SEQRES 28 D 354 ALA LEU ILE
FORMUL 5 HOH *1712(H2 O)
HELIX 1 1 ASP A 31 GLN A 36 1 6
HELIX 2 2 THR A 37 GLN A 43 5 7
HELIX 3 3 ASP A 50 SER A 56 1 7
HELIX 4 4 VAL A 67 ASP A 69 5 3
HELIX 5 5 VAL A 113 ASN A 116 5 4
HELIX 6 6 ASN A 117 HIS A 129 1 13
HELIX 7 7 PRO A 146 ASP A 163 1 18
HELIX 8 8 SER A 174 LEU A 190 1 17
HELIX 9 9 GLY A 213 ASP A 217 5 5
HELIX 10 10 ASP A 217 PHE A 221 5 5
HELIX 11 11 ILE A 224 SER A 226 5 3
HELIX 12 12 GLN A 227 VAL A 250 1 24
HELIX 13 13 SER A 262 GLN A 266 5 5
HELIX 14 14 PHE A 285 ALA A 299 1 15
HELIX 15 15 TYR A 322 ILE A 337 1 16
HELIX 16 16 ASP B 31 GLN B 36 1 6
HELIX 17 17 THR B 37 GLN B 43 5 7
HELIX 18 18 ASP B 50 SER B 58 1 9
HELIX 19 19 VAL B 67 ASP B 69 5 3
HELIX 20 20 VAL B 113 ASN B 116 5 4
HELIX 21 21 ASN B 117 HIS B 129 1 13
HELIX 22 22 PRO B 146 ASP B 163 1 18
HELIX 23 23 SER B 174 LEU B 190 1 17
HELIX 24 24 GLY B 213 ASP B 217 5 5
HELIX 25 25 ASP B 217 PHE B 221 5 5
HELIX 26 26 ILE B 224 SER B 226 5 3
HELIX 27 27 GLN B 227 VAL B 250 1 24
HELIX 28 28 SER B 262 GLN B 266 5 5
HELIX 29 29 PHE B 285 ALA B 299 1 15
HELIX 30 30 TYR B 322 ILE B 337 1 16
HELIX 31 31 ASP C 31 GLN C 36 1 6
HELIX 32 32 THR C 37 GLN C 43 5 7
HELIX 33 33 ASP C 50 GLY C 57 1 8
HELIX 34 34 VAL C 67 ASP C 69 5 3
HELIX 35 35 VAL C 113 ASN C 116 5 4
HELIX 36 36 ASN C 117 HIS C 129 1 13
HELIX 37 37 PRO C 146 ASP C 163 1 18
HELIX 38 38 SER C 174 LEU C 190 1 17
HELIX 39 39 GLY C 213 ASP C 217 5 5
HELIX 40 40 ASP C 217 PHE C 221 5 5
HELIX 41 41 ILE C 224 SER C 226 5 3
HELIX 42 42 GLN C 227 VAL C 250 1 24
HELIX 43 43 SER C 262 GLN C 266 5 5
HELIX 44 44 PHE C 285 ALA C 299 1 15
HELIX 45 45 TYR C 322 ILE C 337 1 16
HELIX 46 46 ASP D 31 GLN D 36 1 6
HELIX 47 47 THR D 37 LYS D 42 5 6
HELIX 48 48 ASP D 50 SER D 56 1 7
HELIX 49 49 VAL D 67 ASP D 69 5 3
HELIX 50 50 VAL D 113 ASN D 116 5 4
HELIX 51 51 ASN D 117 HIS D 129 1 13
HELIX 52 52 PRO D 146 ASP D 163 1 18
HELIX 53 53 ALA D 175 LEU D 190 1 16
HELIX 54 54 GLY D 213 ASP D 217 5 5
HELIX 55 55 ASP D 217 PHE D 221 5 5
HELIX 56 56 ILE D 224 SER D 226 5 3
HELIX 57 57 GLN D 227 VAL D 250 1 24
HELIX 58 58 SER D 262 GLN D 266 5 5
HELIX 59 59 PHE D 285 ALA D 299 1 15
HELIX 60 60 TYR D 322 ALA D 335 1 14
SHEET 1 AA10 ILE A 7 VAL A 11 0
SHEET 2 AA10 VAL A 14 LYS A 19 -1 O VAL A 14 N VAL A 11
SHEET 3 AA10 THR A 303 TYR A 308 1 O THR A 303 N VAL A 15
SHEET 4 AA10 THR A 275 GLY A 280 1 O THR A 275 N THR A 304
SHEET 5 AA10 ILE A 195 LEU A 201 1 O GLN A 198 N THR A 276
SHEET 6 AA10 MET A 167 ASP A 173 1 O ILE A 168 N ASN A 196
SHEET 7 AA10 THR A 99 PHE A 104 1 O VAL A 100 N THR A 169
SHEET 8 AA10 GLU A 131 ASP A 136 1 O GLU A 131 N LEU A 101
SHEET 9 AA10 ARG A 83 PRO A 92 -1 O SER A 86 N ASP A 136
SHEET 10 AA10 VAL A 71 ALA A 80 -1 O THR A 72 N THR A 91
SHEET 1 BA10 ILE B 7 VAL B 11 0
SHEET 2 BA10 VAL B 14 LYS B 19 -1 O VAL B 14 N VAL B 11
SHEET 3 BA10 THR B 303 TYR B 308 1 O THR B 303 N VAL B 15
SHEET 4 BA10 THR B 275 GLY B 280 1 O THR B 275 N THR B 304
SHEET 5 BA10 ILE B 195 LEU B 201 1 O GLN B 198 N THR B 276
SHEET 6 BA10 MET B 167 ASP B 173 1 O ILE B 168 N ASN B 196
SHEET 7 BA10 THR B 99 PHE B 104 1 O VAL B 100 N THR B 169
SHEET 8 BA10 GLU B 131 ASP B 136 1 O GLU B 131 N LEU B 101
SHEET 9 BA10 ARG B 83 PRO B 92 -1 O SER B 86 N ASP B 136
SHEET 10 BA10 VAL B 71 ALA B 80 -1 O THR B 72 N THR B 91
SHEET 1 CA10 ILE C 7 VAL C 11 0
SHEET 2 CA10 VAL C 14 LYS C 19 -1 O VAL C 14 N VAL C 11
SHEET 3 CA10 THR C 303 TYR C 308 1 O THR C 303 N VAL C 15
SHEET 4 CA10 THR C 275 GLY C 280 1 O THR C 275 N THR C 304
SHEET 5 CA10 ILE C 195 LEU C 201 1 O GLN C 198 N THR C 276
SHEET 6 CA10 MET C 167 ASP C 173 1 O ILE C 168 N ASN C 196
SHEET 7 CA10 THR C 99 PHE C 104 1 O VAL C 100 N THR C 169
SHEET 8 CA10 GLU C 131 ASP C 136 1 O GLU C 131 N LEU C 101
SHEET 9 CA10 ARG C 83 PRO C 92 -1 O SER C 86 N ASP C 136
SHEET 10 CA10 VAL C 71 ALA C 80 -1 O THR C 72 N THR C 91
SHEET 1 DA10 ILE D 7 VAL D 11 0
SHEET 2 DA10 VAL D 14 LYS D 19 -1 O VAL D 14 N VAL D 11
SHEET 3 DA10 THR D 303 TYR D 308 1 O THR D 303 N VAL D 15
SHEET 4 DA10 THR D 275 GLY D 280 1 O THR D 275 N THR D 304
SHEET 5 DA10 ILE D 195 PRO D 203 1 O GLN D 198 N THR D 276
SHEET 6 DA10 MET D 167 SER D 174 1 O ILE D 168 N ASN D 196
SHEET 7 DA10 THR D 99 PHE D 104 1 O VAL D 100 N THR D 169
SHEET 8 DA10 GLU D 131 ASP D 136 1 O GLU D 131 N LEU D 101
SHEET 9 DA10 ARG D 83 PRO D 92 -1 O SER D 86 N ASP D 136
SHEET 10 DA10 VAL D 71 ALA D 80 -1 O THR D 72 N THR D 91
CISPEP 1 ALA A 140 PRO A 141 0 -2.02
CISPEP 2 ALA A 145 PRO A 146 0 3.84
CISPEP 3 ALA B 140 PRO B 141 0 -4.69
CISPEP 4 ALA B 145 PRO B 146 0 5.25
CISPEP 5 ALA C 140 PRO C 141 0 -1.20
CISPEP 6 ALA C 145 PRO C 146 0 2.15
CISPEP 7 ALA D 140 PRO D 141 0 -3.09
CISPEP 8 ALA D 145 PRO D 146 0 6.69
CRYST1 168.340 168.340 184.200 90.00 90.00 90.00 I 4 32
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.005940 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005940 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005429 0.00000
TER 2611 ILE A 337
TER 5226 ILE B 337
TER 7865 ILE C 337
TER 10484 ILE D 337
MASTER 732 0 0 60 40 0 0 612192 4 0 112
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